MAFB_MOUSE
ID MAFB_MOUSE Reviewed; 323 AA.
AC P54841; Q3U3C8; Q3UPT9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transcription factor MafB;
DE Short=Maf-B;
DE AltName: Full=Kreisler;
DE AltName: Full=Segmentation protein Kr;
DE AltName: Full=Transcription factor Maf-1;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog B;
GN Name=Mafb; Synonyms=Krml, Maf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8001130; DOI=10.1016/0092-8674(94)90033-7;
RA Cordes S.P., Barsh G.S.;
RT "The mouse segmentation gene kr encodes a novel basic domain-leucine zipper
RT transcription factor.";
RL Cell 79:1025-1034(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10721736; DOI=10.1016/s0378-1119(99)00500-4;
RA Huang K., Serria M.S., Nakabayashi H., Nishi S., Sakai M.;
RT "Molecular cloning and functional characterization of the mouse mafB
RT gene.";
RL Gene 242:419-426(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=10383433; DOI=10.1074/jbc.274.27.19254;
RA Kawauchi S., Takahashi S., Nakajima O., Ogino H., Morita M., Nishizawa M.,
RA Yasuda K., Yamamoto M.;
RT "Regulation of lens fiber cell differentiation by transcription factor c-
RT Maf.";
RL J. Biol. Chem. 274:19254-19260(1999).
RN [8]
RP FUNCTION, AND INTERACTION WITH ETS1.
RX PubMed=10790365; DOI=10.1093/emboj/19.9.1987;
RA Kelly L.M., Englmeier U., Lafon I., Sieweke M.H., Graf T.;
RT "MafB is an inducer of monocytic differentiation.";
RL EMBO J. 19:1987-1997(2000).
RN [9]
RP FUNCTION.
RX PubMed=11823429; DOI=10.1093/emboj/21.3.365;
RA Manzanares M., Nardelli J., Gilardi-Hebenstreit P., Marshall H.,
RA Giudicelli F., Martinez-Pastor M.T., Krumlauf R., Charnay P.;
RT "Krox20 and kreisler co-operate in the transcriptional control of segmental
RT expression of Hoxb3 in the developing hindbrain.";
RL EMBO J. 21:365-376(2002).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=14513037; DOI=10.1038/nn1129;
RA Blanchi B., Kelly L.M., Viemari J.-C., Lafon I., Burnet H., Bevengut M.,
RA Tillmanns S., Daniel L., Graf T., Hilaire G., Sieweke M.H.;
RT "MafB deficiency causes defective respiratory rhythmogenesis and fatal
RT central apnea at birth.";
RL Nat. Neurosci. 6:1091-1100(2003).
RN [11]
RP INTERACTION WITH LRP1, AND SUBCELLULAR LOCATION.
RX PubMed=15135046; DOI=10.1016/j.febslet.2004.03.069;
RA Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M.,
RA Willnow T.E.;
RT "Low-density lipoprotein receptor-related protein interacts with MafB, a
RT regulator of hindbrain development.";
RL FEBS Lett. 565:23-27(2004).
RN [12]
RP FUNCTION, DNA-BINDING, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16443760; DOI=10.2337/diabetes.55.02.06.db05-0946;
RA Artner I., Le Lay J., Hang Y., Elghazi L., Schisler J.C., Henderson E.,
RA Sosa-Pineda B., Stein R.;
RT "MafB: an activator of the glucagon gene expressed in developing islet
RT alpha- and beta-cells.";
RL Diabetes 55:297-304(2006).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16847325; DOI=10.1128/mcb.00001-06;
RA Moriguchi T., Hamada M., Morito N., Terunuma T., Hasegawa K., Zhang C.,
RA Yokomizo T., Esaki R., Kuroda E., Yoh K., Kudo T., Nagata M., Greaves D.R.,
RA Engel J.D., Yamamoto M., Takahashi S.;
RT "MafB is essential for renal development and F4/80 expression in
RT macrophages.";
RL Mol. Cell. Biol. 26:5715-5727(2006).
RN [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=16943423; DOI=10.1128/mcb.00245-06;
RA Aziz A., Vanhille L., Mohideen P., Kelly L.M., Otto C., Bakri Y.,
RA Mossadegh N., Sarrazin S., Sieweke M.H.;
RT "Development of macrophages with altered actin organization in the absence
RT of MafB.";
RL Mol. Cell. Biol. 26:6808-6818(2006).
RN [15]
RP FUNCTION, SUBUNIT, INTERACTION WITH PAX6, DNA-BINDING, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=17901057; DOI=10.1074/jbc.m702795200;
RA Gosmain Y., Avril I., Mamin A., Philippe J.;
RT "Pax-6 and c-Maf functionally interact with the alpha-cell-specific DNA
RT element G1 in vivo to promote glucagon gene expression.";
RL J. Biol. Chem. 282:35024-35034(2007).
RN [16]
RP FUNCTION, SUMOYLATION AT LYS-32 AND LYS-297, AND MUTAGENESIS OF LYS-32 AND
RP LYS-297.
RX PubMed=17548468; DOI=10.1128/mcb.01811-06;
RA Tillmanns S., Otto C., Jaffray E., Du Roure C., Bakri Y., Vanhille L.,
RA Sarrazin S., Hay R.T., Sieweke M.H.;
RT "SUMO modification regulates MafB-driven macrophage differentiation by
RT enabling Myb-dependent transcriptional repression.";
RL Mol. Cell. Biol. 27:5554-5564(2007).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=17360442; DOI=10.1073/pnas.0700013104;
RA Artner I., Blanchi B., Raum J.C., Guo M., Kaneko T., Cordes S., Sieweke M.,
RA Stein R.;
RT "MafB is required for islet beta cell maturation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3853-3858(2007).
RN [18]
RP FUNCTION, MUTAGENESIS OF ASN-248, AND DISRUPTION PHENOTYPE.
RX PubMed=18199433; DOI=10.1016/j.ydbio.2007.12.009;
RA Nishimura W., Rowan S., Salameh T., Maas R.L., Bonner-Weir S., Sell S.M.,
RA Sharma A.;
RT "Preferential reduction of beta cells derived from Pax6-MafB pathway in
RT MafB deficient mice.";
RL Dev. Biol. 314:443-456(2008).
RN [19]
RP DEVELOPMENTAL STAGE.
RX PubMed=17977745; DOI=10.1016/j.mcn.2007.09.006;
RA Saul S.M., Brzezinski J.A. IV, Altschuler R.A., Shore S.E., Rudolph D.D.,
RA Kabara L.L., Halsey K.E., Hufnagel R.B., Zhou J., Dolan D.F., Glaser T.;
RT "Math5 expression and function in the central auditory system.";
RL Mol. Cell. Neurosci. 37:153-169(2008).
RN [20]
RP REVIEW, AND FUNCTION.
RX PubMed=19143053; DOI=10.1038/nrc2460;
RA Eychene A., Rocques N., Pouponnot C.;
RT "A new MAFia in cancer.";
RL Nat. Rev. Cancer 8:683-693(2008).
RN [21]
RP FUNCTION.
RX PubMed=19440205; DOI=10.1038/emboj.2009.127;
RA Smink J.J., Begay V., Schoenmaker T., Sterneck E., de Vries T.J., Leutz A.;
RT "Transcription factor C/EBPbeta isoform ratio regulates osteoclastogenesis
RT through MafB.";
RL EMBO J. 28:1769-1781(2009).
RN [22]
RP DISRUPTION PHENOTYPE.
RX PubMed=27181683; DOI=10.1016/j.ajhg.2016.03.023;
RA Park J.G., Tischfield M.A., Nugent A.A., Cheng L., Di Gioia S.A.,
RA Chan W.M., Maconachie G., Bosley T.M., Summers C.G., Hunter D.G.,
RA Robson C.D., Gottlob I., Engle E.C.;
RT "Loss of MAFB function in humans and mice causes Duane syndrome, aberrant
RT extraocular muscle innervation, and inner-ear defects.";
RL Am. J. Hum. Genet. 98:1220-1227(2016).
CC -!- FUNCTION: Acts as a transcriptional activator or repressor. Plays a
CC pivotal role in regulating lineage-specific hematopoiesis by repressing
CC ETS1-mediated transcription of erythroid-specific genes in myeloid
CC cells. Required for monocytic, macrophage, osteoclast, podocyte and
CC islet beta cell differentiation. Involved in renal tubule survival and
CC F4/80 maturation. Activates the insulin and glucagon promoters.
CC Together with PAX6, transactivates weakly the glucagon gene promoter
CC through the G1 element. SUMO modification controls its transcriptional
CC activity and ability to specify macrophage fate. Binds element G1 on
CC the glucagon promoter. Involved either as an oncogene or as a tumor
CC suppressor, depending on the cell context. Required for the
CC transcriptional activation of HOXB3 in the rhombomere r5 in the
CC hindbrain (PubMed:11823429). {ECO:0000250|UniProtKB:Q9Y5Q3,
CC ECO:0000269|PubMed:10790365, ECO:0000269|PubMed:11823429,
CC ECO:0000269|PubMed:16443760, ECO:0000269|PubMed:16847325,
CC ECO:0000269|PubMed:17548468, ECO:0000269|PubMed:17901057,
CC ECO:0000269|PubMed:18199433, ECO:0000269|PubMed:19143053,
CC ECO:0000269|PubMed:19440205}.
CC -!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription
CC factors. Forms homodimers and heterodimers with FOS, FOSB and FOSL2,
CC but not with JUN proteins (JUN, JUNB and JUND). Interacts with the
CC intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction
CC results in a moderate reduction of MAFB transcriptional potential (By
CC similarity). Binds DNA as a homodimer or a heterodimer. Interacts with
CC PAX6; the interaction is direct. Interacts with ETS1 and LRP1.
CC {ECO:0000250, ECO:0000269|PubMed:10790365, ECO:0000269|PubMed:15135046,
CC ECO:0000269|PubMed:17901057}.
CC -!- INTERACTION:
CC P54841; P01101: Fos; NbExp=4; IntAct=EBI-16093217, EBI-4288185;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:15135046}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreatic alpha-cells (glucagon-
CC positive cells), in podocytes of the kidney and macrophages (at protein
CC level). Most abundant in kidney, gut, lung and brain.
CC {ECO:0000269|PubMed:16443760, ECO:0000269|PubMed:16847325,
CC ECO:0000269|PubMed:17901057}.
CC -!- DEVELOPMENTAL STAGE: Expressed in pancreatic alpha-cells at 10.5 dpc
CC (PubMed:17901057). Expressed in insulin and glucagon islet progenitor
CC cells at 12 dpc onwards (at protein level) (PubMed:16443760).
CC Detectable at 8.0 dpc (one somite) as a band in the caudal hindbrain
CC and by 8.5 dpc (six to eight somites) as a sharp rostral edge
CC coincident with the rhombomeres (r) 4 and 5 boundary and a diffuse
CC caudal edge located midway through r6 (PubMed:8001130). Expressed in
CC the lens epithelial cells at 10.5 to 14.5 dpc (PubMed:10383433).
CC Expressed in the cochlear nucleus at 15.5 dpc (PubMed:17977745).
CC {ECO:0000269|PubMed:10383433, ECO:0000269|PubMed:16443760,
CC ECO:0000269|PubMed:17901057, ECO:0000269|PubMed:17977745,
CC ECO:0000269|PubMed:8001130}.
CC -!- DOMAIN: The leucine-zipper domain is involved in the interaction with
CC LRPICD.
CC -!- PTM: Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its
CC transcriptional repression activity and promotes macrophage
CC differentiation from myeloid progenitors.
CC {ECO:0000269|PubMed:17548468}.
CC -!- DISRUPTION PHENOTYPE: Mice show a defect in frequency of respiratory
CC rhythm with a fatal apnea at birth due to lack of neurons from the
CC preBoetC region. They displayed renal dysgenesis with abnormal podocyte
CC differentiation as well as tubular apoptosis. They show altered actin-
CC dependent macrophage morphology. They show a reduced number of cells
CC expressing insulin and glucagon. Embryos also lack the abducens nerve
CC which normaly innervates the lateral rectus muscle that is involved in
CC eye movement (PubMed:27181683). {ECO:0000269|PubMed:14513037,
CC ECO:0000269|PubMed:16847325, ECO:0000269|PubMed:16943423,
CC ECO:0000269|PubMed:17360442, ECO:0000269|PubMed:18199433,
CC ECO:0000269|PubMed:27181683}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; L36435; AAA65689.1; -; mRNA.
DR EMBL; AF180338; AAD56221.1; -; Genomic_DNA.
DR EMBL; AK132425; BAE21161.1; -; mRNA.
DR EMBL; AK143209; BAE25306.1; -; mRNA.
DR EMBL; AK154830; BAE32860.1; -; mRNA.
DR EMBL; AL591665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06288.1; -; Genomic_DNA.
DR EMBL; BC016434; AAH16434.1; -; mRNA.
DR EMBL; BC038256; AAH38256.1; -; mRNA.
DR CCDS; CCDS16994.1; -.
DR PIR; I49529; I49529.
DR RefSeq; NP_034788.1; NM_010658.3.
DR PDB; 2WT7; X-ray; 2.30 A; B=214-303.
DR PDB; 2WTY; X-ray; 2.90 A; A/B=211-306.
DR PDB; 4AUW; X-ray; 2.90 A; A/B/E/F=211-305.
DR PDBsum; 2WT7; -.
DR PDBsum; 2WTY; -.
DR PDBsum; 4AUW; -.
DR AlphaFoldDB; P54841; -.
DR SMR; P54841; -.
DR BioGRID; 201014; 5.
DR DIP; DIP-60663N; -.
DR IntAct; P54841; 2.
DR STRING; 10090.ENSMUSP00000096728; -.
DR iPTMnet; P54841; -.
DR PhosphoSitePlus; P54841; -.
DR MaxQB; P54841; -.
DR PaxDb; P54841; -.
DR PeptideAtlas; P54841; -.
DR PRIDE; P54841; -.
DR ProteomicsDB; 287292; -.
DR Antibodypedia; 956; 311 antibodies from 33 providers.
DR DNASU; 16658; -.
DR Ensembl; ENSMUST00000099126; ENSMUSP00000096728; ENSMUSG00000074622.
DR GeneID; 16658; -.
DR KEGG; mmu:16658; -.
DR UCSC; uc008nqw.2; mouse.
DR CTD; 9935; -.
DR MGI; MGI:104555; Mafb.
DR VEuPathDB; HostDB:ENSMUSG00000074622; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000160486; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; P54841; -.
DR OMA; ESHQPLH; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; P54841; -.
DR TreeFam; TF325689; -.
DR BioGRID-ORCS; 16658; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mafb; mouse.
DR PRO; PR:P54841; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P54841; protein.
DR Bgee; ENSMUSG00000074622; Expressed in molar tooth and 235 other tissues.
DR Genevisible; P54841; MM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0021599; P:abducens nerve formation; IMP:UniProtKB.
DR GO; GO:0035284; P:brain segmentation; IMP:MGI.
DR GO; GO:1903575; P:cornified envelope assembly; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISO:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IMP:MGI.
DR GO; GO:0021571; P:rhombomere 5 development; IMP:MGI.
DR GO; GO:0021572; P:rhombomere 6 development; IMP:MGI.
DR GO; GO:0007379; P:segment specification; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013592; Maf_TF_N.
DR InterPro; IPR028571; MafB.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF10; PTHR10129:SF10; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR Pfam; PF08383; Maf_N; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW Proto-oncogene; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..323
FT /note="Transcription factor MafB"
FT /id="PRO_0000076495"
FT DOMAIN 238..301
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 34..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..263
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 266..287
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 50..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:17548468"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:17548468"
FT MUTAGEN 32
FT /note="K->R: Loss of SUMO modification, increases
FT transactivation activity, increases macrophage
FT differentiation and inhibits myeloid progenitor growth;
FT when associated with R-297."
FT /evidence="ECO:0000269|PubMed:17548468"
FT MUTAGEN 248
FT /note="N->A: Reduces ability to activate insulin and
FT glucagon gene expression."
FT /evidence="ECO:0000269|PubMed:18199433"
FT MUTAGEN 248
FT /note="N->S: Loss of transcriptional activity."
FT /evidence="ECO:0000269|PubMed:18199433"
FT MUTAGEN 297
FT /note="K->R: Loss of SUMO modification, increases
FT transactivation activity, increases macrophage
FT differentiation and inhibits myeloid progenitor growth;
FT when associated with R-32."
FT /evidence="ECO:0000269|PubMed:17548468"
FT CONFLICT 275
FT /note="Q -> K (in Ref. 3; BAE32860)"
FT /evidence="ECO:0000305"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:2WT7"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:2WT7"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2WTY"
FT HELIX 233..299
FT /evidence="ECO:0007829|PDB:2WT7"
SQ SEQUENCE 323 AA; 35809 MW; D77AE07ABD9C2AD2 CRC64;
MAAELSMGQE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ PAGSVSSTPL
STPCSSVPSS PSFSPTEPKT HLEDLYWMAS NYQQMNPEAL NLTPEDAVEA LIGSHPVPQP
LQSFDGFRSA HHHHHHHHPH PHHGYPGAGV THDDLGQHAH PHHHHHHQAS PPPSSAASPA
QQLPTSHPGP GPHATAAATA AGGNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK
QKRRTLKNRG YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK
LANSGFREAG STSDSPSSPE FFL
